{PDOC51700}
{PS51700; SEPARIN}
{BEGIN}
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* SEPARIN core domain profile *
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In eukaryotic  cells, replicated DNA strands remain physically connected until
their segregation  to opposite poles of the cell during anaphase. This "sister
chromatid cohesion"  is  essential  for  the  alignment  of chromosomes on the
mitotic spindle during metaphase. Cohesion depends on the multisubunit cohesin
complex, which  possibly  forms  the  physical bridges connecting sisters. The
separins (separases) cleave the Scc1p subunit of the cohesin complex, allowing
the separation of sister chromatids in anaphase. Separins are highly conserved
in all eukaryotes but have not been detected in prokaryotes [1,2].

All known  separin  homologs  possess a conserved C-terminal "separin" domain.
The separin  core  domain  contains a conserved histidine and cyteine residue,
which are  hallmarks  of cysteine proteases. These two residues are invariably
surrounded by  small  residues  (glycine  or  serine), and each is preceded by
amino acid  sequences that are predicted to form hydrophobic beta sheets. This
pattern is  characteristic  of  cysteine  endopeptidases  of the CD clan [E1],
which includes  caspases,  legumains, gingipains, clostripains, anf GPI-anchor
amidases. The  histidine  end cysteine residues are likely to form the separin
domain's catalytic dyad [1,2]. The separin core domain forms the peptidase C50
family [E2].

The profile we developed covers the entire SEPARIN core domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2014 / First entry.

[ 1] Uhlmann F., Wernic D., Poupart M.-A., Koonin E.V., Nasmyth K.
     "Cleavage of cohesin by the CD clan protease separin triggers anaphase
     in yeast."
     Cell 103:375-386(2000).
     PubMed=11081625
[ 2] Aravind L., Koonin E.V.
     "Classification of the caspase-hemoglobinase fold: detection of new
     families and implications for the origin of the eukaryotic separins."
     Proteins 46:355-367(2002).
     PubMed=11835511
[E1] https://www.ebi.ac.uk/merops/cgi-bin/clansum?clan=CD
[E1] https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=C50

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